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Activation and specificity of alkaline phosphatase of a mineralizing collagen-rich system
Abstract:
Alkaline phosphatase from tibia tendon of Meleagris gallopavo L. was highly purified. The enzyme activation by different ions was measured. Mg2+ showed a high activation with a broader spectrum of phosphomonoester hydrolization. The in vivo Mg2+ concentration was an optimum for in vitro activation.